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cDNA cloning, characterization and stable expression of novel human brain carboxylesterase
Author(s) -
Mori Mieko,
Hosokawa Masakiyo,
Ogasawara Yuko,
Tsukada Eiko,
Chiba Kan
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01111-4
Subject(s) - carboxylesterase , catalytic triad , isozyme , gene , endoplasmic reticulum , complementary dna , biochemistry , hydrolase , molecular cloning , chemistry , biology , peptide sequence , microbiology and biotechnology , enzyme
The DNA sequence encoding a novel human brain carboxylesterase (CES) has been determined. The protein is predicted to have 567 amino acids, including conserved motifs, such as GE AGG, GXXXX FG, and GD GD which comprise a catalytic triad, and the endoplasmic reticulum retention motif (HXEL‐COOH) observed in CES families. Their gene products exhibited hydrolase activity towards temocapril, p ‐nitrophenylacetate and long‐chain acyl‐CoA. Since the molecular masses of these gene products are similar to those that exist in capillary endothelial cells of the human brain [Yamamda et al. (1994) Brain Res. 658, 163–167], these CES isozymes may function as a blood‐brain barrier to protect the central nervous system from ester or amide compounds.